Optically active lysine derivatives, such as an optically active 6,6-dimethyl lysine derivative of the formula (3) wherein * means an asymmetric carbon atom, P1 and P2 are each independently an amino-protecting group or hydrogen atom where P1 and P2 are not hydrogen atoms at the same time, or P1 and P2 in combination show an amino-protecting group, and P4 is a hydrogen atom or carboxyl-protecting group, and an optically active lysine derivative of the formula (5) wherein *, P1 and P2 are as defined above, R1 is alkyl group having 1 to 6 carbon atoms or aralkyl group having 7 to 12 carbon atoms, and P5 is a hydrogen atom or carboxyl-protecting group, are useful as pharmaceutical intermediates.
For example, a compound having an S-configuration of asymmetric carbon atom is an important intermediate compound for a pharmaceutical compound of the following formula (25), which is useful as an antihypertensive agent having an inhibitory activity against an angiotensin converting enzyme (ACE) and neutral endopeptidase (NEP) (Journal of Medicinal Chemistry, 1999, 42, 305–311). 
As a method for producing the pharmaceutical compound of the formula (25), Journal of Medicinal Chemistry, 1999, 42, 305–311 discloses a method shown by the following scheme using (s)-2-phthalimido-6-hydroxyhexanoic acid as a starting material. 
However, this method requires many steps, and there is a demand on a production method that permits easier and simpler industrial production.
It is also known that an optically active amino acid can be generated by directly applying a microorganism enzyme system to 5-substituted hydantoin as a starting material. When a microorganism enzyme system is used, an enzyme (hydantoinase) to hydrolyze a 5-substituted hydantoin compound and produce N-carbamyl-amino acid, and an enzyme (N-carbamyl-amino-acid hydrolase) to enantio-selectively decompose the produced N-carbamyl-amino acid into optically active amino acid are required.
Conventionally, there are methods for producing D-amino acid using microorganisms containing these two kinds of enzymes, or substances containing such enzymes, such as a method comprising the use of bacteria of the genus Pseudomonas (JP-B-56-003034), a method comprising the use of bacteria of the genus Agrobacterium (JP-A-03-019696) and the like.
As a method for producing L-amino acid, there are known a method comprising the use of bacteria of the genus Flavobacterium (JP-B-56-008749), a method comprising the use of bacteria of the genus Bacillus (JP-A-63-24895), a method comprising the use of bacteria of the genus Pseudomonas (JP-A-01-071476), a method comprising the use of bacteria of the genus Arthrobacter [J. Biotechnol., Vol. 46, p. 63 (1996)] and the like.
It has been also reported that optically active amino acid can be produced by isolating a genetic DNA of hydantoinase and a genetic DNA of N-carbamyl-amino-acid hydrolase from various bacteria and expressing them in E. coli [Biotechnol. Prog., vol. 16, p. 564 (2000), EP515698 and the like].
It has been detailed that the substrate specificity of these hydantoinase and N-carbamyl-amino-acid hydrolase is rather broad, and by a combined use of these two kinds of enzymes under the limitation of the substrate specificity, natural or nonnatural various amino acids having optical activity can be produced from 5-substituted hydantoin compound [Enzyme Catalysis in Organic Synthesis, K. Drauz et al. ed., vol. 1, ch. B2.4, pp. 409–431, VCH (1995)]. Because the producible optically active amino acid is limited due to its substrate specificity, however, an optically active amino acid corresponding to 5-substituted hydantoin compound is not always generated. For example, Microbacterium liquefaciens AJ3940 strain (formerly classified under Flavobacteriuim sp.) that affords L-tryptophan in a high yield from 5-indolylmethylhydantoin (racemate) acts well on 5-substituted hydantoin having an aromatic ring, and can generate many kinds of L-enantiomer of aromatic amino acids such as L-phenylalanine, L-tyrosine and the like. However, since it does not act at all on 5-methylhydantoin, 5-sec-butylhydantoin, 5-carboxymethylhydantoin or 5-carboxyethylhydantoin, and does not produce the corresponding L-alanine, L-isoleucine, L-aspartic acid or L-glutamic acid, it is known to be specific to compounds having an aromatic ring [Agric. Biol. Chem., vol. 51, p. 729 (1987)].